H-FQNALLVR^-OH

Ref. 3D-PP47396

Información del producto

• Nombre: H-FQNALLVR^-OH

Descripción

Peptide H-FQNALLVR^-OH is a Research Peptide with significant interest within the field academic and medical research. This peptide is available for purchase at Cymit Quimica in multiple sizes and with a specification of your choice. Recent citations using H-FQNALLVR^-OH include the following: Formation of c1 fragment ions in collision-induced dissociation of glutamine-containing peptide ions: a tip for de novo sequencing YJ Lee , YM Lee - Rapid communications in mass spectrometry, 2004 - Wiley Online Libraryhttps://analyticalsciencejournals.onlinelibrary.wiley.com/doi/abs/10.1002/rcm.1593 Peptide Mapping of Human Serum Albumin Modified Minimally by Methylglyoxal in Vitro and in Vivo N Ahmed, PJ Thornalley - Annals of the New York Academy of , 2005 - Wiley Online Libraryhttps://nyaspubs.onlinelibrary.wiley.com/doi/abs/10.1196/annals.1333.031 Peptide mapping identifies hotspot site of modification in human serum albumin by methylglyoxal involved in ligand binding and esterase activity N Ahmed, D Dobler, M Dean, PJ Thornalley - Journal of Biological , 2005 - ASBMBhttps://www.jbc.org/article/S0021-9258(19)63076-0/abstract Quantitative bottom-up proteomics depends on digestion conditions MS Lowenthal, Y Liang, KW Phinney - Analytical , 2014 - ACS Publicationshttps://pubs.acs.org/doi/abs/10.1021/ac4027274 Reaction of human albumin with aspirin in vitro: mass spectrometric identification of acetylated lysines 199, 402, 519, and 545 MS Liyasova, LM Schopfer, O Lockridge - Biochemical pharmacology, 2010 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0006295209009010 Enhanced analyte detection using in-source fragmentation of field asymmetric waveform ion mobility spectrometry-selected ions in combination with time-of-flight LJ Brown, RW Smith, DE Toutoungi - Analytical , 2012 - ACS Publicationshttps://pubs.acs.org/doi/abs/10.1021/ac300212r Exploiting charge differences for the analysis of challenging post-translational modifications by capillary electrophoresis-mass spectrometry K Faserl, B Sarg , V Maurer, HH Lindner - Journal of Chromatography A, 2017 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0021967317301802 Absolute Quantification of the Lower Abundance Proteome through Immunoaffinity Depletion of the twenty most abundant proteins in human serum JJ Porter, J Wildsmith, CD Melm, MD Schuchard - , 2022 - sigmaaldrich.comhttps://www.sigmaaldrich.com/US/en/deepweb/assets/sigmaaldrich/product/documents/578/044/hupoaqua.pdf Identification of the amino acids of human serum albumin involved in the reaction with the naproxen acyl coenzyme A thioester using liquid chromatography combined J Olsen, I Bjornsdottir, J Tjornelund, SH Hansen - Analytical biochemistry, 2003 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0003269702004621 BTK-inhibitor drug covalent binding to lysine in human serum albumin using LC-MS/MS C Muste, C Gu - Drug Metabolism and Pharmacokinetics, 2022 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S1347436721000549 Proteomics Study on Cross-linking Reaction of Formaldehyde and HSA B Li, DY Hu, XL Xin, R Lan, YL Deng - Advanced Materials , 2012 - Trans Tech Publhttps://www.scientific.net/AMR.343-344.1035 Multiplexed MRM-based quantitation of candidate cancer biomarker proteins in undepleted and non-enriched human plasma AJ Percy , AG Chambers, J Yang, CH Borchers - Proteomics, 2013 - Wiley Online Libraryhttps://analyticalsciencejournals.onlinelibrary.wiley.com/doi/abs/10.1002/pmic.201200316

• Marca: Biosynth